MolNFT v1 · #15298 · protein

Crystal structure of ferrochelatase with cadmium bound at active site

1N0I: “Crystal structure of ferrochelatase with cadmium bound at active site”. X-ray diffraction, 3 ligands (MG, CD, CL), 1 pocket (best druggability 0.78). MolNFT v1 #15298 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1N0I
Type: protein
Length: 309 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferrochelatase
EC: 4.99.1.1
UniProt: P32396
Ligands: MG, CD, CL
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferrochelatase (EC 4.99.1.1)	protein	309	49% helix, 17% strand	P32396

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A
CD · Cadmium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	536	0.78	0.85	58	CD, MG

Compared structures

1N0I · Crystal Structure of Ferrochelatase with Cadmium bound at active site · the same entry in another collection · chain A against A, TM-score 1.00
P32396 · AlphaFold monomer V2.0 prediction for coproporphyrin III ferrochelatase (P32396) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P32396
Elsewhere: RCSB PDB 1N0I · PDBe 1N0I · UniProt P32396

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